一种与酿酒酵母中的转录因子IIF相互作用的C末端结构域磷酸酶的重要组成部分。
An essential component of a C-terminal domain phosphatase that interacts with transcription factor IIF in Saccharomyces cerevisiae.
作者信息
Archambault J, Chambers R S, Kobor M S, Ho Y, Cartier M, Bolotin D, Andrews B, Kane C M, Greenblatt J
机构信息
Banting and Best Department of Medical Research, University of Toronto, 112 College Street, Toronto, Ontario, Canada M5G 1L6.
出版信息
Proc Natl Acad Sci U S A. 1997 Dec 23;94(26):14300-5. doi: 10.1073/pnas.94.26.14300.
Abstract
One of the essential components of a phosphatase that specifically dephosphorylates the Saccharomyces cerevisiae RNA polymerase II (RPII) large subunit C-terminal domain (CTD) is a novel polypeptide encoded by an essential gene termed FCP1. The Fcp1 protein is localized to the nucleus, and it binds the largest subunit of the yeast general transcription factor IIF (Tfg1). In vitro, transcription factor IIF stimulates phosphatase activity in the presence of Fcp1 and a second complementing fraction. Two distinct regions of Fcp1 are capable of binding to Tfg1, but the C-terminal Tfg1 binding domain is dispensable for activity in vivo and in vitro. Sequence comparison reveals that residues 173-357 of Fcp1 correspond to an amino acid motif present in proteins of unknown function predicted in many organisms.
摘要
一种特异性使酿酒酵母RNA聚合酶II（RPII）大亚基C端结构域（CTD）去磷酸化的磷酸酶的重要组成部分是一个由名为FCP1的必需基因编码的新型多肽。Fcp1蛋白定位于细胞核，并且它与酵母通用转录因子IIF（Tfg1）的最大亚基结合。在体外，转录因子IIF在Fcp1和第二个互补组分存在的情况下刺激磷酸酶活性。Fcp1的两个不同区域能够与Tfg1结合，但C端Tfg1结合结构域对于体内和体外活性而言是可有可无的。序列比较显示，Fcp1的173 - 357位残基对应于在许多生物体中预测的功能未知的蛋白质中存在的一个氨基酸基序。
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